Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Help & Advice
University of Warwick

The Library

  • Login
  • Admin

Spatial structure of the decapeptide Val-Ile-Lys-Lys-Ser-Thr-Ala-Leu-Leu-Gly in water and in a complex with sodium dodecyl sulfate micelles

Tools
- Tools
+ Tools

Blokhin, D. S., Efimov, S. V., Klochkov, A. V., Yulmetov, A. R., Filippov, A. V., Antzutkin, Oleg N., Aganov, A. V. and Klochkov, V. V. (2011) Spatial structure of the decapeptide Val-Ile-Lys-Lys-Ser-Thr-Ala-Leu-Leu-Gly in water and in a complex with sodium dodecyl sulfate micelles. Applied Magnetic Resonance, Vol.41 (No.2-4). pp. 267-282. doi:10.1007/s00723-011-0257-x

Research output not available from this repository, contact author.
Official URL: http://dx.doi.org/10.1007/s00723-011-0257-x

Request Changes to record.

Abstract

We have studied the spatial structure of the decapeptide Val-Ile-LysLys-Ser-Thr-Ala-Leu-Leu-Gly in aqueous solution and in a complex with sodium dodecyl sulfate (SDS) micelles by (1)H nuclear magnetic resonance (NMR) spectroscopy and two-dimensional (2-D) NMR spectroscopy (total correlation spectroscopy and nuclear Overhauser effect spectroscopy (NOESY)). The approach used to determine the decapeptide spatial structure was based on analysis of the (1)H-(13)C residual dipolar couplings in the molecules partially aligned in lyotropic liquid crystalline media. Analysis of the interproton distances obtained from the 2-D NOESY NMR spectrum was used to reveal the spatial structure of the decapeptide in a complex with SDS micelles. Complex formation was confirmed by analysis of (1)H chemical shifts in the NMR spectrum of the decapeptide and analysis of the signs and values of NOEs in a solution with SDS micelles.

Item Type: Journal Article
Subjects: Q Science > QC Physics
Divisions: Faculty of Science, Engineering and Medicine > Science > Physics
Journal or Publication Title: Applied Magnetic Resonance
Publisher: Springer
ISSN: 0937-9347
Official Date: December 2011
Dates:
DateEvent
December 2011Published
Volume: Vol.41
Number: No.2-4
Page Range: pp. 267-282
DOI: 10.1007/s00723-011-0257-x
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access
Funder: Russian Foundation for Basic Research , Ministry of Education and Science of the Russian Federation
Grant number: 09-03-00077a (Russian Foundation for Basic Research), 02.740.11.0702 (Ministry of Education and Science of the Russian Federation)

Data sourced from Thomson Reuters' Web of Knowledge

Request changes or add full text files to a record

Repository staff actions (login required)

View Item View Item
twitter

Email us: wrap@warwick.ac.uk
Contact Details
About Us